Purification and Characterization of Flammulin, a Basic Protein with Anti-tumor Activities from Flammulina velutipes

摘要

Aim To purify and characterize flammulin, a basic protein with anti-tumor activities. Methods Ammonium sulfate, ethanol fractionation and column chromatography were used for separation and purification. Electrophoretic analysis, amino acid analysis, and MS of flammulin were carried out. Results Flammulin was purified to electrophoretic homogeneity and crystallized. With a molecular mass of 19891.13 Da, pI 8.9, λ_(max) = 276 - 278 nm, λ_(min) = 250 nm, flammulin was characterized by its lack of methionine. Fingerprint mapping of flammulin was determined by MALDI-MS following in-gel protease digestion; no close matches were identified. Conclusion Flammulin was purified to electrophoretic homogeneity, and its characteristics are discussed for the first time.